http://www.cnr.it/ontology/cnr/individuo/prodotto/ID305302
Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors (Articolo in rivista)
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- Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1039/c2cc34275h (literal)
- Alternative label
Di Fiore, Anna; Maresca, Alfonso; Supuran, Claudiu T.; De Simone, Giuseppina (2012)
Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors
in Chemical communications (Lond., 1996, Print)
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- Di Fiore, Anna; Maresca, Alfonso; Supuran, Claudiu T.; De Simone, Giuseppina (literal)
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- ISI Web of Science (WOS) (literal)
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- University of Florence; Istituto di Biostrutture e Bioimmagini-Consiglio Nazionale delle Ricerche (CNR) (literal)
- Titolo
- Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors (literal)
- Abstract
- Hydroxamates (R-CONHOH) have been scarcely investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs). An inhibition/structural study of PhCONHOH is reported against all human isoforms. Comparing aliphatic (R = Me and CF3) and aromatic (R = Ph) hydroxamates as CAIs, we prove that CONHOH is a versatile zinc binding group. Depending on the nature of the R moiety, it can adopt different coordination modes to the catalytic ion within the CA active site. (literal)
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